Search PubMed⌕ Search

Biomedical subjects

T Isobe

Publications and source records attributed to T Isobe.

At least 235 records · Page 13Linked to original sources
PubMed1984

Reverse cellular distribution of calmodulin to S-100 protein in primate brain.

Both calmodulin and S-100 protein are Ca2+-binding proteins of the EF-hand family. Immunocytochemical study revealed that calmodulin existed mainly in the neurons, whereas S-100 protein was localized primarily in the glial cells of the cerebral and cerebellar cortices of man and monkey. The observed reverse cellular distribution of calmodulin to S-100 protein in primate brain suggests that calmodulin might be replaced in its role as a Ca2+-binding protein by S-100 protein in the glial cells.

Animals↗
PubMed1984

The alpha subunit of S100 protein is present in tumor cells of human malignant melanoma, but not in schwannoma.

The subunits of S100 protein were isolated from surgically resected tissues of human malignant melanoma and schwannoma by means of an affinity chromatography followed by high performance liquid chromatography. The melanoma tissue gave rise to the alpha and beta subunits in almost equal quantities while the schwannoma tissue yielded only the beta subunit, indicating that the S100 subunits were distributed differently between these tumor tissues. This finding suggests that the cellular distribution of S100 subunits varies, so that the cells containing S100 protein can be classified into several types on the basis of the subunit composition.

Amino Acids↗
PubMed1984

The nucleotide sequence of a complete chicken delta-crystallin cDNA.

The nucleotide sequence of a full length cDNA of delta-crystallin mRNA from chicken lens has been determined using a delta-crystallin cDNA clone (pB delta 11), which represents the mRNA sequence of 1530 nucleotides from the poly(A) junction but does not contain the 5'-terminal sequence of 44 nucleotides of the mRNA. The 5'-terminal sequence of the mRNA, absent in the cDNA clone, has been determined with a stretch of cDNA sequence by the primer extension procedure. The amino acid sequence deduced from the nucleotide sequence is consistent with the amino acid sequences of several tryptic peptides, the total amino acid composition, and the mol. wt. of delta-crystallin estimated by SDS-polyacrylamide gel electrophoresis. The computer-assisted analysis predicts high alpha-helical content throughout the polypeptide. Sequence analyses have revealed that gene 1 encodes the mRNA from which the cDNA clone was derived.

Amino Acid Sequence↗
PubMed1984

Detection of S-100 protein in melanocytic and neurogenic cutaneous tumors.

Quantitative determination of S-100 protein content on human melanoma tissues and in sera of melanoma patients was made possible through radioimmunoassay (RIA). Melanoma tissue extracts prepared from metastatic sites in both skin and lymph nodes contained 0.08-2.80% of S-100 out of the total extractable proteins, and it was also noticed that the tumors obtained from lymph-node metastasis possessed slightly higher levels of S-100 as compared with those obtained from the skin lesions. Serum S-100 levels of 12 melanoma patients with Stage 1 to 3 diseases were also examined by means of RIA, but only two patients showed a slight elevation of serum S-100 levels. When tissue sections prepared from a variety of cutaneous tumors, including pigmented nevus, melanoma and Schwannoma, were stained for S-100 by an immunoperoxidase technique, these tumors of neuroectodermal origin were demonstrated to contain a detectable amount of S-100, whereas other tested nonmelanocytic and non-neurogenic tumors were entirely negative for S-100. These data stress the usefulness of S-100 for the diagnosis of neurogenic and melanocytic tumors, especially melanomas, despite the difficulty of its detection in the sera of the tumor bearers, which might reflect the low tendency of S-100 to be shed from the tumor cells.

Humans↗
PubMed1984

Immunohistochemical study on the distribution of alpha and beta subunits of S-100 protein in human neoplasm and normal tissues.

The immunohistochemical distribution and localization of the alpha and beta subunits of S-100 protein in human neoplasms and normal tissues were studied by the PAP method using monospecific rabbit antibodies against each subunit. Beta subunit immunoreactivity was detected in all S-100-positive cells and tumors reported previously. In contrast alpha subunit immunoreactivity was absent from Schwann cells, schwannomas, neurofibromas, granular cell myoblastomas, pituicytes of the neurohypophysis, Langerhans cells, interdigitating reticulum cells, and histiocytosis X cells. Interestingly, only the alpha subunit was detected in neurons of both central and peripheral nervous system, and in lymph node macrophages. Human S-100-positive cells are divided into three groups; the first is composed of cells containing only the beta subunit (probably S-100b; beta beta), the second consists of cells containing both the alpha and beta subunits, and the third is composed of cells containing only the alpha subunit (probably S- 100ao ; alpha alpha). The ontogentic relationships between S-100-positive cells and tumors are discussed in the light of these findings.

Biomarkers↗
PubMed1984

Large scale preparation and crystallization of neuron-specific enolase.

A simple method has been developed for the large scale purification of neuron-specific enolase [EC 4.2.1.11]. The method consists of ammonium sulfate fractionation of brain extract, and two subsequent column chromatography steps on DEAE Sephadex A-50. The chromatography was performed on a short (25 cm height) and thick (8.5 cm inside diameter) column unit that was specially devised for the large scale preparation. The purified enolase was crystallized in 0.05 M imidazole-HCl buffer containing 1.6 M ammonium sulfate (pH 6.39), with a yield of 0.9 g/kg of bovine brain tissue.

Amino Acids↗
PubMed1984

S100a0 (alpha alpha) protein is present in neurons of the central and peripheral nervous system.

The cellular distribution of S100 subunits in human brain and peripheral nerves was studied by means of an immunohistochemical technique using antibodies specific to the alpha subunit or the beta subunit of S100 protein. The results indicate that the distribution of the alpha subunit and the beta subunit is different among cell types in the nervous tissue, and that neurons in the brain and peripheral nerves contain only the alpha subunit, or S100a0 protein. The subunit distribution also appears to be different at an intracellular level, where the immunoreaction products for the alpha subunit show granular arrangement whereas those for the beta subunit are found diffusely in the cytoplasm.

Animals↗
PubMed1984

Development of second generation merozoites of Leucocytozoon caulleryi in vitro.

Sporozoites of Leucocytozoon caulleryi were inoculated into specific-pathogen-free (SPF) chickens intravenously. Fourteen days after inoculation, the infected blood, parasitized with second generation merozoites, was collected from the chickens. The blood was then suspended in SPF chicken serum or RPMI-1640 culture medium supplemented with 20% SPF chicken serum in petri dishes, which were cultured at 37 degrees C or 41 degrees C in a humidified atmosphere of 5% CO2. Second generation merozoites in parasitized, immature erythrocytes developed continuously through several substages and finally became micro- and macro-gametocytes after 6 days of incubation.

Animals↗
PubMed1984

Bullous amyloidosis associated with Bence Jones proteinemia without proteinuria.

A 74 yo female was found to have bullous dermal amyloidosis on the background of systemic amyloidosis with multiple myeloma. There was monoclonal immunoglobulin light chain of kappa type in the serum with no proteinuria (Bence Jones proteinemia without Bence Jones proteinuria), along with proliferations of kappa-producing plasma cells in the marrow.

Aged↗
PubMed1984

[S 100 protein].

Explore the source record for details and available documents.

Amino Acid Sequence↗
PubMed1984

Immunohistochemical localization and distribution of S-100 proteins in the human lymphoreticular system.

Immunohistochemical localization of S-100b protein and S-100ao protein in human lymphoreticular system was studied by using monospecific antibody directed against either the alpha subunit or beta subunit of S-100 protein. S-100b protein immunoreactivity was detected in Langerhans cells, interdigitating reticulum cells, and histiocytosis X cells, but not in ordinary macrophages and blood monocytes. In contrast, S-100ao protein immunoreactivity was detected in blood monocytes, macrophages of lymph node, alveolar macrophages of lung, and small numbers of Kupffer cells of liver. S-100ao immunoreactivity was also detected in epithelioid cells, Langhans giant cells, and foreign body giant cells. The present findings suggest that the presence of S-100ao protein in the cytoplasm is one of the characteristic features of cells in the human mononuclear phagocyte system. The detection of S-100b, but not S-100ao, immunoreactivity in Langerhans cells and interdigitating reticulum cells also suggests that they are independent of the monocyte-macrophage system. S-100ao protein may be a novel cytoplasmic marker for cells of the human monocyte-macrophage system.

Biomarkers↗
PubMed1983

A new immunoglobulin marker.

In an examination of 16 human immunoglobulin lambda-light chains, one was found to have amino acid substitutions which have not previously been reported for the constant region of the lambda-chains. It involved in two positions: an arginine instead of lysine at position 130, and a leucine for glutamine at position 195 (Sh numbering (1) ). The structural variation is tentatively designated as "Is" marker.

Amino Acid Sequence↗
PubMed1983

Developmental changes in the translatable mRNA for beta subunit of S-100 protein in rat brain.

The presence of mRNA coding for beta subunit of S-100 protein was demonstrated in polyadenylated RNA from the rat brain in vitro translation in a reticulocyte lysate cell-free system. The products were identified with S-100 protein beta subunit using the immunoprecipitation of the reaction products with the specific antisera, comigration of the isolated, labelled peptide with the purified S-100 protein in SDS-polyacrylamide gel electrophoresis and fluorography and the same retention time of the labelled S-100 protein beta subunit with authentic S-100 beta subunit by high performance liquid chromatography. The size determination of mRNA for S-100 protein on sucrose density gradient centrifugation gave 6-8 S. The assay gave a linear response with increasing amounts of polyadenylated RNA, allowing quantitation of mRNA level for S-100 protein in polyadenylated RNA. During the prenatal period and 10 postnatal days, only minute amounts of mRNA for beta subunit of S-100 protein could be found, however a dramatic increase of mRNA for beta subunit of S-100 was observed within the period of 10 to about 30 days and the mRNA level maintained a plateau from 40 days to adult age. These date indicate that the development changes in the amount of S-100 protein in the rat brain found by other authors is strongly correlated with the changes in the level of its translatable mRNA.

Aging↗
PubMed1983

CT diagnosis of common bile duct stone.

Common bile duct stones were demonstrated as high-density objects on CT in 22 of 45 cases. About 96% of the remaining cases (22 of 23) exhibited other abnormal CT findings which included common bile duct dilatation, concomitant gallbladder stones, and/or presence of intraductal air. CT is a useful diagnostic modality in the elevation of patients with suspected choledocholithiasis.

Adult↗
PubMed1983

A case of corneal amyloidosis.

An unilateral case of corneal amyloidosis, presenting the clinical appearance and histopathological findings of a gelatinous drop-like corneal dystrophy in a 59-year-old male was reported. In the specimen obtained by a penetrating keratoplasty, amyloid was confirmed with light and electron microscopy. On the basis of histopathological findings, the origin of amyloid appeared to be closely related to the fibroblasts.

Amyloid↗